Klaus Schulten (January 12, 1947 – October 31, 2016) was a German-American computational biophysicist and the Swanlund Professor of Physics at the University of Illinois at Urbana-Champaign.
[3] Schulten used supercomputing techniques to apply theoretical physics to the fields of biomedicine and bioengineering and dynamically model living systems.
[4] His mathematical, theoretical, and technological innovations led to key discoveries about the motion of biological cells, sensory processes in vision, animal navigation, light energy harvesting in photosynthesis, and learning in neural networks.
His research group developed and distributed software for computational structural biology, which Schulten used to make a number of significant discoveries.
Schulten was able to provide a theoretical explanation for experimental observations of an "optically forbidden" state which did not match predicted patterns of electronic excitation in polyenes.
One of his first projects was to explain a chemical reaction product called a "fast triplet", an excited molecule with a pair of electrons with parallel spins.
[14] Schulten and others have since extended this early work, developing a model of the possible excitation of cryptochrome proteins in photoreceptors within the retina of the eye.
In 1988, Hartmut Michel, Johann Deisenhofer, and Robert Huber won the Nobel Prize in chemistry for determining the three-dimensional structure of the photosynthetic reaction center.
[19] In 1988, Schulten moved to the University of Illinois at Urbana-Champaign (UIUC), where he founded the Theoretical and Computational Biophysics Group at the Beckman Institute for Advanced Science and Technology in 1989.
[3][20] The early development of NAMD at UIUC built on the work of Schulten's students in Munich to build a custom parallel computer optimized for molecular dynamics simulations.
[24] Validation of models against experimental results is an integral part of development, for example, using molecular dynamics in combination with cryo-electron microscopy and X-ray crystallography.
[30] A 2009 review describes work in modeling and verifying simulations of proteins such as titin, fibrinogen, ankyrin, and cadherin using the group's "computational microscope".
Modeling the processes involved in converting sunlight into chemical energy meant representing 100 million atoms, 16,000 lipids, and 101 proteins, the contents of a tiny sphere-shaped organelle occupying just one percent of the cell's total volume.
[5] He received the Biophysical Society Distinguished Service Award for 2013, for "laying the groundwork for the realistic molecular dynamic simulations of biological macromolecules on time scales that match the physiological realm, and for making the methods and software openly available.